ArticleJournal of molecular biology2020
Dissecting the Functional Contributions of the Intrinsically Disordered C-terminal Tail of Bacillus subtilis FtsZ.
Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- Functional flexibility in bacterial hub proteins is driven by proteome expansion.Scientific reports · 2026Article
- Phosphorylation of a conserved intrinsically disordered region is necessary for activation of a bacterial Hanks-type Ser/Thr kinase signaling pathway.bioRxiv : the preprint server for biology · 2025Article
- High-throughput discovery of inhibitory protein fragments with AlphaFold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- High-throughput discovery of inhibitory protein fragments with AlphaFold.bioRxiv : the preprint server for biology · 2024Article
- Evolution of a minimal cell.Nature · 2023Article
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- MipZ caps the plus-end of FtsZ polymers to promote their rapid disassembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Uncovering the molecular mechanism for dual effect of ATP on phase separation in FUS solution.Science advances · 2022Article
- Conformational buffering underlies functional selection in intrinsically disordered protein regions.Nature structural & molecular biology · 2022Article
- A conceptual framework for understanding phase separation and addressing open questions and challenges.Molecular cell · 2022Review
- Competing interactions give rise to two-state behavior and switch-like transitions in charge-rich intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease.Protein science : a publication of the Protein Society · 2022Article
- The Regulatory Roles of Intrinsically Disordered Linker in VRN1-DNA Phase Separation.International journal of molecular sciences · 2022Article
- How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?Frontiers in microbiology · 2022Review
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- α-tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics.Developmental cell · 2021Article
- Antistaphylococcal Activity of the FtsZ Inhibitor C109.Pathogens (Basel, Switzerland) · 2021Article
- Intrachain interaction topology can identify functionally similar intrinsically disordered proteins.Biophysical journal · 2021Article
- The emergence of phase separation as an organizing principle in bacteria.Biophysical journal · 2021Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
FtsZ is a bacterial GTPase that is central to the spatial and temporal control of cell division. It is a filament-forming enzyme that encompasses a well-folded core domain and a disordered C-terminal tail (CTT). The CTT is essential for ensuring proper assembly of the cytokinetic ring, and its deletion leads to mis-localization of FtsZ, aberrant assembly, and cell death. In this work, we dissect the contributions of modules within the disordered CTT to assembly and enzymatic activity of Bacillus subtilis FtsZ (Bs-FtsZ). The CTT features a hypervariable C-terminal linker (CTL) and a conserved C-terminal peptide (CTP). Our in vitro studies show that the CTL weakens the driving forces for forming single-stranded active polymers and suppresses lateral associations of these polymers, whereas the CTP promotes the formation of alternative assemblies. Accordingly, in full-length Bs-FtsZ, the CTL acts as a spacer that spatially separates the CTP sticker from the core, thus ensuring filament formation through core-driven polymerization and lateral associations through CTP-mediated interactions. We also find that the CTL weakens GTP binding while enhancing the catalytic rate, whereas the CTP has opposite effects. The joint contributions of the CTL and CTP make Bs-FtsZ, an enzyme that is only half as efficient as a truncated version that lacks the CTT. Overall, our data suggest that the CTT acts as an auto-regulator of Bs-FtsZ assembly and as an auto-inhibitor of enzymatic activity. Based on our results, we propose hypotheses regarding the hypervariability of CTLs and compare FtsZs to other bacterial proteins with tethered IDRs.
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